Studies of the ceruloplasmin-lactoferrin complex
doi: 10.1139/o01-206
pmid: 11908641
Studies of the ceruloplasmin-lactoferrin complex
We have previously shown that iron-containing human lactoferrin (LF) purified from breast milk is able to form both in vitro and in vivo a complex with ceruloplasmin (CP), the copper-containing protein of human plasma. Here we present evidence that the CP–LF complex is dissociated by high concentrations of NaCl, CaCl2, or EDTA, or by decreasing the pH to 4.7. In addition, DNA, bacterial lipopolysaccharide, and heparin can displace CP from its complex with LF. Antibodies to either of the two proteins also cause dissociation of the complex.Key words: lactoferrin, ceruloplasmin, ferroxidase.
- Institute of Experimental Medicine Russian Federation
- Department of Medical Sciences Russian Federation
Milk, Human, Macromolecular Substances, Ceruloplasmin, Hydrogen-Ion Concentration, Sodium Chloride, Chromatography, Affinity, Calcium Chloride, Lactoferrin, Chromatography, Gel, Humans, Electrophoresis, Polyacrylamide Gel, Edetic Acid, Protein Binding
Milk, Human, Macromolecular Substances, Ceruloplasmin, Hydrogen-Ion Concentration, Sodium Chloride, Chromatography, Affinity, Calcium Chloride, Lactoferrin, Chromatography, Gel, Humans, Electrophoresis, Polyacrylamide Gel, Edetic Acid, Protein Binding
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